Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Search research articles

Related Experiment Video

Updated: Jun 6, 2026

Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer

Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer

Published on: August 2, 2018

Practical 4'-phosphopantetheine active site discovery from proteomic samples.

Jordan L Meier¹, Anand D Patel, Sherry Niessen

¹Department of Chemistry and Biochemistry, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California at San Diego, La Jolla California 92093, USA.

Journal of Proteome Research

|November 12, 2010

Summary

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Proteomic discovery of chemical probes that perturb protein complexes in human cells.

Molecular cell·2023

Same author

Remodeling oncogenic transcriptomes by small molecules targeting NONO.

Nature chemical biology·2023

Same author

Depletion of creatine phosphagen energetics with a covalent creatine kinase inhibitor.

Nature chemical biology·2023

Same author

Glutathione supports lipid abundance <i>in vivo</i>.

bioRxiv : the preprint server for biology·2023

Same author

TMEM164 is an acyltransferase that forms ferroptotic C20:4 ether phospholipids.

Nature chemical biology·2023

Same author

Author Correction: Selective inhibitors of JAK1 targeting an isoform-restricted allosteric cysteine.

Nature chemical biology·2022

Researchers developed new proteomic methods to detect 4'-phosphopantetheine (PPant) peptides, crucial for natural product biosynthesis. These advancements enable the study of polyketide synthase (PKS) and nonribosomal peptide synthetase (NRPS) enzymes in proteomic settings.

Area of Science:

Biochemistry and Molecular Biology
Natural Product Discovery
Proteomics

Background:

Polyketides and nonribosomal peptides are vital natural products with significant biological activities.
Polyketide synthases (PKS) and nonribosomal peptide synthetases (NRPS) are key enzymes in their biosynthesis.
Detecting the 4"-phosphopantetheine (PPant) modification on these enzymes via proteomics is challenging due to low abundance and instability.

Purpose of the Study:

To develop novel experimental and computational strategies for identifying PPant peptides in shotgun proteomics.
To overcome limitations in detecting this crucial post-translational modification.
To enable the study of PKS/NRPS enzymes and natural product biosynthesis in a proteomic context.

Main Methods:

More Related Videos

Oligopeptide Competition Assay for Phosphorylation Site Determination

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Related Experiment Videos

Last Updated: Jun 6, 2026

Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer

Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer

Published on: August 2, 2018

Oligopeptide Competition Assay for Phosphorylation Site Determination

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Activity-based enrichment to increase the MS input of PKS/NRPS-related peptides.

Targeted fragmentation strategies to identify potential PPant active sites.

An enhanced data analysis pipeline for direct identification and validation of PPant peptides from MS² data.

A machine learning approach for direct PPant peptide detection from MS² fragmentation data.

Main Results:

Successful development of methods to address experimental and computational challenges in PPant peptide detection.
Demonstrated ability to identify and validate PPant peptides using MS² data.
A novel machine learning model capable of directly detecting PPant peptides from fragmentation data.

Conclusions:

The developed methods facilitate the practical discovery of the PPant post-translational modification.
These advancements represent a significant step towards studying natural product biosynthesis using proteomic approaches.
The study provides new tools for analyzing a previously cryptic post-translational modification.